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Phosphate esters characterization

In humans, thiamine is both actively and passively absorbed to a limited level in the intestines, is transported as the free vitamin, is then taken up in actively metabolizing tissues, and is converted to the phosphate esters via ubiquitous thiamine kinases. During thiamine deficiency all tissues stores are readily mobilhed. Because depletion of thiamine levels in erythrocytes parallels that of other tissues, erythrocyte thiamine levels ate used to quantitate severity of the deficiency. As deficiency progresses, thiamine becomes indetectable in the urine, the primary excretory route for this vitamin and its metaboHtes. Six major metaboHtes, of more than 20 total, have been characterized from human urine, including thiamine fragments (7,8), and the corresponding carboxyHc acids (1,37,38). [Pg.88]

Phosphonates are organic phosphates characterized by a C-P-O bond, which is much more resistant to hydrolysis than the polyphosphate bond (O-P-O) or the phosphate ester bond (C-O-P), making them suitable for many types of BW treatment formulation. Phosphonates were originally developed for the industrial and institutional (I I) cleaning market in the 1960s, but are commonly employed in a myriad of applications. [Pg.448]

In addition to their poor solubility in water, alkyl phosphate esters and dialkyl phosphate esters are further characterized by sensitivity to water hardness [37]. A review of the preparation, properties, and uses of surface-active anionic phosphate esters prepared by the reactions of alcohols or ethoxylates with tetra-phosphoric acid or P4O10 is given in Ref. 3. The surfactant properties of alkyl phosphates have been investigated [18,186-188]. The critical micelle concentration (CMC) of the monoalkyl ester salts is only moderate see Table 6 ... [Pg.591]

A structurally characterized example of a dinuclear zinc complex with a bridging phosphate monoester was provided by Kitajima and co-workers using the tris(pyrazolyl)borate ligand system. The P—O bond in a tris- or bis-phosphate ester is cleaved by a hydroxo zinc complex resulting in the monoester compound.443... [Pg.1183]

Kimura and co-workers have made a major contribution to this area with dizinc azamacrocycle complexes characterized including phosphate ester X-ray structures.445,446 They have also studied ligands with pendent alcohol groups.44... [Pg.1183]

Corrano and co-workers have characterized phosphate ester species with a mixed donor heteroscorpionate tripod zinc species 452 Krebs and co-workers synthesized purple acid phosphatase mimics including a structurally characterized FemZnn phosphate bridged dimeric species.453... [Pg.1183]

A wide range of anionic surfactants (Fig. 23) has been classified into groups, including alkyl benzene sulfonates (ABS), linear alkyl benzene sulfonates (LAS), alcohol sulfates (AS), alcohol ether sulfates (AES), alkyl phenol ether sulfates (APES), fatty acid amide ether sulfates (FAES), alpha-olefin sulfates (AOS), paraffin sulfonates, alpha sulfonated fatty acids and esters, sulfonated fatty acids and esters, mono- and di-ester sulfosuccinates, sulfosuccinamates, petroleum sulfonates, phosphate esters, and ligno-sulfonates. Of the anionic surfactants, ABS and LAS continue to be the major products of anionic surfactants [314, 324]. Anionic surfactants have been extensively monitored and characterized in various environmental matrices [34,35,45,325-329]. [Pg.51]

The recognition that the Mo in the molybdoproteins exists in organic cofactor forms came from studies of mutants of Aspergillus and Neurospora.650 In 1964, Pateman and associates discovered mutants that lacked both nitrate reductase and xanthine dehydrogenase. Later, it was shown that acid-treated molybdoenzymes released a material that would restore activity to the inactived nitrate reductase from the mutant organisms. This new coenzyme, a phosphate ester of molybdopterin (Fig. 15-17), was characterized by Rajagopalan and coworkers.650 651 A more complex form of the coenzyme, molybdopterin cytosine dinucleotide... [Pg.891]

The preceding experiments prove that there is an intermediate on the reaction pathway in each case, the measured rate constants for the formation and decay of the intermediate are at least as high as the value of kcat for the hydrolysis of the ester in the steady state. They do not, however, prove what the intermediate is. The evidence for covalent modification of Ser-195 of the enzyme stems from the early experiments on the irreversible inhibition of the enzyme by organo-phosphates such as diisopropyl fluorophosphate the inhibited protein was subjected to partial hydrolysis, and the peptide containing the phosphate ester was isolated and shown to be esterified on Ser-195.1516 The ultimate characterization of acylenzymes has come from x-ray diffraction studies of nonspecific acylenzymes at low pH, where they are stable (e.g., indolylacryloyl-chymotrypsin),17 and of specific acylenzymes at subzero temperatures and at low pH.18 When stable solutions of acylenzymes are restored to conditions under which they are unstable, they are found to react at the required rate. These experiments thus prove that the acylenzyme does occur on the reaction pathway. They do not rule out, however, the possibility that there are further intermediates. For example, they do not rule out an initial acylation on His-57 followed by rapid intramolecular transfer. Evidence concerning this and any other hypothetical intermediates must come from additional kinetic experiments and examination of the crystal structure of the enzyme. [Pg.122]

Swinkels29 collected published characterization data for tapioca starch and compared it to that for other starches of commercial significance (Table 12.4). Tapioca starch is differentiated from other starches by its low level of residual materials (fat, protein, ash), lower amylose content than for other amylose-containing starches, and high molecular weights of amylose and amylopectin. The small amount of phosphorus in tapioca starch is partially removable30 and, therefore, not bound as the phosphate ester as in potato starch. It is also common to find protein and lipid values of zero, as reported by Hicks.31 The very low protein and lipid content is an important factor which differentiates tapioca starch from the cereal starches. [Pg.550]

Moses, V, Ferrier, R.J., and Calvin, M., 1962, Characterization of the photosynthetically synthesized y-keto phosphate ester of 2-keto-L-gulonic acid. Proc. Natl. Acad. Sci. U.S.A. 48 1644-1652. [Pg.43]

In this case, cleavage of the phosphate ester bond occurs by an unusual reaction mechanism however, the structure of the substrate allows a facile /3-elimination reaction that is characterized by a lower activation energy barrier than attack of a nucleophile on an anionic phosphate ester. [Pg.136]

The purple acid phosphatases (PAP) catalyze the hydrolysis of phosphate esters under acidic pH conditions (pH optimum 5) (9, 10). They differ from other acid phosphatases in having a distinct purple color due to the presence of iron or manganese and in being uninhibited by tartrate. Diiron units have been found in the active sites of the enzymes from mammalian spleen (171-173) and uterus (173, 174), while a heterodinu-clear FeZn unit has been characterized for the enzyme from red kidney bean (175). Either the Fe2 or the FeZn unit is catalytically competent in these enzymes, since the enzymes from porcine uterus and bovine spleen can be converted into active FeZn forms and the kidney bean enzyme can be transformed into an active Fe2 form (176). There are also enzymes from other plant sources (particularly sweet potato) that have been reported to have either a mononuclear Mn(III) or Fe(III) active site (177), but these are beyond the scope of the review. This section will focus on the enzymes from porcine uterus (also called uteroferrin), bovine spleen, and red kidney bean. [Pg.149]

As noted in the introduction, the effects of multiple modes of catalysis are often multiplicative rather than simply additive. Consequently, it is not surprising that a number of hydrolytic metalloenzymes have evolved that utilize a constellation of three metal ions in catalysis. Perhaps not coincidentally, all well-characterized examples of this class catalyze the hydrolytic cleavage of phosphate ester or phosphoric acid anhydride bonds, which represent a difficult and long-standing chemical problem. In every case but one, the metal ions in the trimetal centers are all zinc. As we shall see, alkaline phosphatase utilizes a Zn2Mg trinuclear center. It should be pointed out that in the older literature many of the enzymes discussed in this section have been described as containing dinuclear metal centers. Only in the last few years has it become clear that three metal ions are present and participate in catalysis by these systems. [Pg.665]


See other pages where Phosphate esters characterization is mentioned: [Pg.322]    [Pg.1215]    [Pg.210]    [Pg.169]    [Pg.292]    [Pg.292]    [Pg.10]    [Pg.322]    [Pg.448]    [Pg.87]    [Pg.311]    [Pg.175]    [Pg.102]    [Pg.367]    [Pg.206]    [Pg.142]    [Pg.142]    [Pg.837]    [Pg.4464]    [Pg.448]    [Pg.182]    [Pg.101]    [Pg.131]    [Pg.126]    [Pg.316]    [Pg.515]    [Pg.836]    [Pg.367]    [Pg.232]    [Pg.6593]    [Pg.313]    [Pg.664]    [Pg.122]   
See also in sourсe #XX -- [ Pg.44 , Pg.45 , Pg.302 ]




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